2ar3

[[Image:2ar3.gif|left|200px]]<br /><applet load="2ar3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2ar3, resolution 2.20&Aring;" />

'''E90A mutant structure of PlyL'''<br />

==Overview==

We report a structural and functional analysis of the lambda prophage Ba02, endolysin (PlyL) encoded by the Bacillus anthracis genome. We show that, PlyL comprises two autonomously folded domains, an N-terminal catalytic, domain and a C-terminal cell wall-binding domain. We determined the, crystal structure of the catalytic domain; its three-dimensional fold is, related to that of the cell wall amidase, T7 lysozyme, and contains a, conserved zinc coordination site and other components of the catalytic, machinery. We demonstrate that PlyL is an N-acetylmuramoyl-L-alanine, amidase that cleaves the cell wall of several Bacillus species when, applied exogenously. We show, unexpectedly, that the catalytic domain of, PlyL cleaves more efficiently than the full-length protein, except in the, case of Bacillus cereus, and using GFP-tagged cell wall-binding domain, we, detected strong binding of the cell wall-binding domain to B. cereus but, not to other species tested. We further show that a related endolysin, (Ply21) from the B. cereus phage, TP21, shows a similar pattern of, behavior. To explain these data, and the species specificity of PlyL, we, propose that the C-terminal domain inhibits the activity of the catalytic, domain through intramolecular interactions that are relieved upon binding, of the C-terminal domain to the cell wall. Furthermore, our data show that, (when applied exogenously) targeting of the enzyme to the cell wall is not, a prerequisite of its lytic activity, which is inherently high. These, results may have broad implications for the design of endolysins as, therapeutic agents.

 

==About this Structure==

2AR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AR3 OCA].

 

==Reference==

Structure and lytic activity of a Bacillus anthracis prophage endolysin., Low LY, Yang C, Perego M, Osterman A, Liddington RC, J Biol Chem. 2005 Oct 21;280(42):35433-9. Epub 2005 Aug 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16103125 16103125]

[[Category: N-acetylmuramoyl-L-alanine amidase]]

[[Category: Single protein]]

[[Category: Liddington, R.C.]]

[[Category: Low, L.Y.]]

[[Category: Osterman, A.]]

[[Category: Perego, M.]]

[[Category: Yang, C.]]